Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Christophe Maris"'
Autor:
Georg Dorn, Christoph Gmeiner, Tebbe de Vries, Emil Dedic, Mihajlo Novakovic, Fred F. Damberger, Christophe Maris, Esteban Finol, Chris P. Sarnowski, Joachim Kohlbrecher, Timothy J. Welsh, Sreenath Bolisetty, Raffaele Mezzenga, Ruedi Aebersold, Alexander Leitner, Maxim Yulikov, Gunnar Jeschke, Frédéric H.-T. Allain
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract RNA-binding proteins (RBPs) are crucial regulators of gene expression, often composed of defined domains interspersed with flexible, intrinsically disordered regions. Determining the structure of ribonucleoprotein (RNP) complexes involving s
Externí odkaz:
https://doaj.org/article/6ecfd082137440199e61e0254d4f1997
Autor:
Sapna Ravindranathan, Christophe Maris, Frédéric H.-T. Allain, Irene Beusch, Fred F. Damberger, Sandrine Jayne, Georg Dorn
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 48 (8)
Nucleic Acids Research, 48 (8)
The polypyrimidine tract binding protein (PTB) is a multi-domain protein involved in alternative splicing, mRNA localization, stabilization, polyadenylation and translation initiation from internal ribosome entry sites (IRES). In this latter process,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4435f9b029bcd3ab160b85236f36781a
https://pubmed.ncbi.nlm.nih.gov/32170319
https://pubmed.ncbi.nlm.nih.gov/32170319
Autor:
Frédéric H.-T. Allain, Stanislaw Dunin-Horkawicz, Inna Grishina, Christophe Maris, Janusz M. Bujnicki, Stéphane Thore, Timm Maier, Albrecht Bindereif, Markus Blatter
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2015, 427 (19), pp.3001-3022. ⟨10.1016/j.jmb.2015.05.020⟩
Journal of Molecular Biology, Elsevier, 2015, 427 (19), pp.3001-3022. ⟨10.1016/j.jmb.2015.05.020⟩
The RNA recognition motif (RRM) is the far most abundant RNA binding domain. In addition to the typical β1α1β2β3α2β4 fold, various sub-structural elements have been described and reportedly contribute to the high functional versatility of RRMs.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2988e1e4a5b5f9db143560616d79d6c8
https://doi.org/10.1016/j.jmb.2015.05.020
https://doi.org/10.1016/j.jmb.2015.05.020
Publikováno v:
Molecular Cell. 41(5):579-588
Summary Splicing of the c-src N1 exon is repressed by the polypyrimidine tract-binding protein (PTB or PTBP1). During exon repression, the U1 snRNP binds properly to the N1 exon 5′ splice site but is made inactive by the presence of PTB. Examining
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40e7705499d373192dcf912b4eb89329
Publikováno v:
RNA (New York N.Y.)
The human hnRNP C is a ubiquitous cellular protein involved in mRNA maturation. Recently, we have shown that this protein specifically recognizes uridine (U) pentamers through its single RNA recognition motif (RRM). However, a large fraction of natur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62c4eb9471483bd5df7c4a4c2dacfde7
https://europepmc.org/articles/PMC4604433/
https://europepmc.org/articles/PMC4604433/
Publikováno v:
The EMBO Journal. 25:2487-2497
Regulatory RNA elements, like riboswitches, respond to intracellular signals by three-dimensional (3D) conformational changes. RNA thermometers employ a similar strategy to sense temperature changes in the cell and regulate the translational machiner
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab23d4025980da8d7a6fe08b39e37b18
https://doi.org/10.1038/sj.emboj.7601128
https://doi.org/10.1038/sj.emboj.7601128
Publikováno v:
FEBS Journal. 272:2118-2131
The RNA recognition motif (RRM), also known as RNA-binding domain (RBD) or ribonucleoprotein domain (RNP) is one of the most abundant protein domains in eukaryotes. Based on the comparison of more than 40 structures including 15 complexes (RRM–RNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15465394b7ac641b4393538e6575cd3e
https://doi.org/10.1111/j.1742-4658.2005.04653.x
https://doi.org/10.1111/j.1742-4658.2005.04653.x
Publikováno v:
RNA. 11:173-186
We have solved the NMR structure of the 31-nucleotide (nt) apoB mRNA stem–loop, a substrate of the cytidine deaminase APOBEC1. We found that the edited base located at the 5′ end of the octa-loop is stacked between two adenosines in both the uned
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::907e40a295ae2a8bc74cf476487b63f9
https://doi.org/10.1261/rna.7190705
https://doi.org/10.1261/rna.7190705
Autor:
Matthew J. Fox, Myeong Y. Chung, Suzanne E. Paulson, Udo Krischke, Christophe Maris, Richard Meller, R. Lueb
Publikováno v:
Atmospheric Environment. 37:149-158
Here we describe the development of a new instrument to measure the total airborne non-methane organic carbon concentration (TNMOC), and the ratio of this value to the sum of speciated volatile organic compounds (VOCs) measured by standard gas chroma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::434caa5529b40dc8538fc95aee834c8f
https://doi.org/10.1016/s1352-2310(03)00387-x
https://doi.org/10.1016/s1352-2310(03)00387-x
Publikováno v:
Atmospheric Environment. 37:159-170
Simultaneous measurements of total non-methane organic carbon (TNMOC) and speciated volatile organic compounds (VOCs) were made with an instrument described in a companion paper. The ratio of the TNMOC to the speciated VOCs measurement indicates the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f48ee9b3f14c682eeecc47e5b7df3890
https://doi.org/10.1016/s1352-2310(03)00388-1
https://doi.org/10.1016/s1352-2310(03)00388-1